Serum Amyloid P-Component

Known as: P Component, Amyloid, Serum Amyloid P Component, P-Component, Serum Amyloid 
Amyloid P component is a small, non-fibrillar glycoprotein found in normal serum and in all amyloid deposits. It has a pentagonal (pentaxin… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1957-2018
010020019572017

Papers overview

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Highly Cited
2015
Highly Cited
2015
BACKGROUND The amyloid fibril deposits that cause systemic amyloidosis always contain the nonfibrillar normal plasma protein… (More)
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Highly Cited
2010
Highly Cited
2010
Accumulation of amyloid fibrils in the viscera and connective tissues causes systemic amyloidosis, which is responsible for about… (More)
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Highly Cited
2002
Highly Cited
2002
The normal plasma protein serum amyloid P component (SAP) binds to fibrils in all types of amyloid deposits, and contributes to… (More)
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Highly Cited
1999
Highly Cited
1999
Serum amyloid P component (SAP), a highly conserved plasma protein named for its universal presence in amyloid deposits, is the… (More)
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Highly Cited
1997
Highly Cited
1997
The tissue amyloid deposits that characterize systemic amyloidosis, Alzheimer's disease and the transmissible spongiform… (More)
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Highly Cited
1995
Highly Cited
1995
Extracellular deposition of amyloid fibrils is responsible for the pathology in the systemic amyloidoses and probably also in… (More)
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Highly Cited
1994
Highly Cited
1994
The three-dimensional structure of pentameric human serum amyloid P component at high resolution, the first reported for a… (More)
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1991
1991
A normal reference interval for serum amyloid P component (SAP) concentration in the serum was established in 500 healthy adult… (More)
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Highly Cited
1990
Highly Cited
1990
BACKGROUND In systemic amyloidosis the distribution and progression of disease have been difficult to monitor, because they can… (More)
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Highly Cited
1979
Highly Cited
1979
Serum amyloid P-component (protein SAP) was found to bind in vitro to isolated amyloid fibrils of both primary and secondary… (More)
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